Journal
MOLECULAR CELL
Volume 10, Issue 5, Pages 1033-1043Publisher
CELL PRESS
DOI: 10.1016/S1097-2765(02)00708-6
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Funding
- NIAID NIH HHS [AI 42200] Funding Source: Medline
- NIGMS NIH HHS [T32 GM 0720] Funding Source: Medline
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First identified as a neutrophil granule component, neutrophil gelatinase-associated lipocalin (NGAL; also called human neutrophil lipocalin, 24p3, uterocalin, or neu-related lipocalin) is a member of the lipocalin family of binding proteins. Putative NGAL ligands, including neutrophil chemotactic agents such as N-formylated tripeptides, have all been refuted by recent biochemical and structural results. NGAL has subsequently been implicated in diverse cellular processes, but without a characterized ligand, the molecular basis of these functions remained mysterious. Here we report that NGAL tightly binds bacterial catecholate-type ferric siderophores through a cyclically permuted, hybrid electrostatic/cation-pi interaction and is a potent bacteriostatic agent in iron-limiting conditions. We therefore propose that NGAL participates in the antibacterial iron depletion strategy of the innate immune system.
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